T. Ohta

发表

Sequence and characteristics of the Bifidobacterium longum gene encoding L-lactate dehydrogenase and the primary structure of the enzyme: a new feature of the allosteric site.

H. Masaki, S. Iwata, T. Minowa, 1989, Gene.

Crystallization of allosteric L-lactate dehydrogenase from Thermus caldophilus and preliminary crystallographic data.

S. Iwata, H. Matsuzawa, T. Ohta, 1991, Journal of biochemistry.

Molecular Basis of Allosteric Activation of Bacterial L-Lactate Dehydrogenase

S. Iwata, T. Ohta, 1993 .

Escherichia coli K-12 tolZ mutants tolerant to colicins E2, E3, D, Ia, and Ib: defect in generation of the electrochemical proton gradient

H. Matsuzawa, T. Ohta, Y. Koyama, 1984, Journal of bacteriology.

Peptidoglycan synthetic activities in membranes of Escherichia coli caused by overproduction of penicillin-binding protein 2 and rodA protein.

B. Spratt, Brian, F. Ishino, 1986, The Journal of biological chemistry.

Genes encoding two lipoproteins in the leuS-dacA region of the Escherichia coli chromosome

H. Kamata, F. Ishino, H. Matsuzawa, 1987, Journal of bacteriology.

Identification of the penicillin-binding active site of penicillin-binding protein 2 of Escherichia coli.

F. Ishino, H. Matsuzawa, M. Matsuhashi, 1988, Journal of biochemistry.

Production of thermophilic protease by glucose-controlled fed-batch culture of recombinant Escherichia coli

H. Matsuzawa, T. Ohta, S. Sakamoto, 1994 .

A thermostable Gm-methylase recognizes the tertiary structure of tRNA.

K. Watanabe, T. Oshima, I. Kumagai, 1987, Journal of biochemistry.

Application of a Metal Switch to Aqualysin I, a Subtilisin-type Bacterial Serine Protease, to the S3 Site Residues, Ser102 and Gly131

H. Matsuzawa, Y. Kikuchi, T. Ohta, 2000, Bioscience, biotechnology, and biochemistry.

NoteApplication of a Metal Switch Serine Protease , to the S 3 Siteto Aqualysin I , a Residues , Serl 02 SS $ A Subtilisin-type Bacterial and Gly 131

Y. Kikuchi, T. Ohta, Terumichi Tanaka, 2022 .

Substrate Specificity of Aqualysin I AItered by an Organic Solvent ,

H. Matsuzawa, T. Ohta, Terumichi Tanaka, 2022 .

Methionyl-tRNA synthetase gene from an extreme thermophile, Thermus thermophilus HB8. Molecular cloning, primary-structure analysis, expression in Escherichia coli, and site-directed mutagenesis.

O. Nureki, K. Suzuki, S. Yokoyama, 1991, The Journal of biological chemistry.

A non-covalent NH2-terminal pro-region aids the production of active aqualysin I (a thermophilic protease) without the COOH-terminal pro-sequence in Escherichia coli.

H. Matsuzawa, T. Ohta, Y. C. Lee, 1992, FEMS microbiology letters.

Molecular cloning and characterization of the genes (pbpA and rodA) responsible for the rod shape of Escherichia coli K-12: analysis of gene expression with transposon Tn5 mutagenesis and protein synthesis directed by constructed plasmids

H. Matsuzawa, M. Matsuhashi, T. Ohta, 1983, Journal of bacteriology.

Binding of Formylmethionyl-tRNA and Aminoacyl-tRNA to Ribosomes

R. Thach, T. Ohta, ROBERT E. THACH, 1968, Nature.

Histidine 296 is essential for the catalysis in Lactobacillus plantarum D-lactate dehydrogenase.

T. Ohta, H. Taguchi, Hayao Taguchi, 1993, The Journal of biological chemistry.

Detection of the conformational change in the catalytic site of adenosine triphosphatase from beef liver mitochondria by affinity labeling with the dialdehyde derivative of ethenoadenosine triphosphate.

T. Wakagi, T. Ohta, 1982, Journal of biochemistry.

A plasmid region encoding the active fragment and the inhibitor protein of colicin E3—CA38

H. Masaki, T. Ohta, 1982, FEBS letters.

Studies on the Structure and Function of Subtilisin E by Protein Engineering

M. Inouye, M. Yamasaki, H. Matsuzawa, 1992, Annals of the New York Academy of Sciences.

Reddish Escherichia coli cells caused by overproduction of Bacillus stearothermophilus uroporphyrinogen III methylase: cloning, sequencing, and expression of the gene.

Y. Sakano, H. Matsuzawa, H. Sakai, 1995, Bioscience, biotechnology, and biochemistry.

Production and Extracellular Secretion of Aqualysin I (a Thermophilic Subtilisin-Type Protease) in a Host-Vector System for Thermus thermophilus

H. Matsuzawa, T. Ohta, Y. Koyama, 1991, Applied and environmental microbiology.

Estimation of Hydrodynamic Volume of Proteins Using High-Performance Size-Exclusion Chromatography and Intrinsic Viscosity Measurement: An Attempt At Universal Calibration

T. Ohta, N. Chikazumi, 1991 .

Unique precursor structure of an extracellular protease, aqualysin I, with NH2- and COOH-terminal pro-sequences and its processing in Escherichia coli.

H. Matsuzawa, T. Ohta, Y. Miyata, 1990, The Journal of biological chemistry.

Purification and characterization of aqualysin I (a thermophilic alkaline serine protease) produced by Thermus aquaticus YT-1.

H. Matsuzawa, T. Ohta, H. Taguchi, 1988, European journal of biochemistry.

Allosteric Activation of L-Lactate Dehydrogenase Analyzed by Hybrid Enzymes with Effector-sensitive and -insensitive Subunits*

S. Iwata, H. Matsuzawa, S. Fushinobu, 1996, The Journal of Biological Chemistry.

Effects of urea on the activity and structure of yeast alcohol dehydrogenase.

T. Ohta, Y. Ogura, 1965, Journal of biochemistry.

Involvement of Glu-264 and Arg-235 in the essential interaction between the catalytic imidazole and substrate for the D-lactate dehydrogenase catalysis.

H. Matsuzawa, T. Ohta, H. Taguchi, 1997, Journal of biochemistry.

Essential role of arginine 235 in the substrate-binding of Lactobacillus plantarum D-lactate dehydrogenase.

T. Ohta, H. Taguchi, 1994, Journal of biochemistry.

D-lactate dehydrogenase is a member of the D-isomer-specific 2-hydroxyacid dehydrogenase family. Cloning, sequencing, and expression in Escherichia coli of the D-lactate dehydrogenase gene of Lactobacillus plantarum.

T. Ohta, T Ohta, H Taguchi, 1991, The Journal of biological chemistry.

PHOTOOXIDATIVE CONSUMPTION AND PHOTOREDUCTIVE FORMATION OF ASCORBIC ACID IN GREEN LEAVES

T. Ohta, A. Mitsui, 1961 .

Colicin E3 and its immunity genes.

H. Masaki, T. Ohta, 1985, Journal of molecular biology.

Molecular structure and immunity specificity of colicin E6, an evolutionary intermediate between E-group colicins and cloacin DF13

H. Masaki, T. Ohta, A. Akutsu, 1989, Journal of bacteriology.

Primary structures of the ColE2-P9 and ColE3-CA38 lysis genes.

H. Masaki, T. Ohta, M. Toba, 1986, Journal of biochemistry.

Immunity Specificity and Evolution of the Nuclease-Type E Colicins

S. Yajima, H. Masaki, T. Uozumi, 1992 .

Heat-stable and fructose 1,6-bisphosphate-activated L-lactate dehydrogenase from an extremely thermophilic bacterium.

H. Matsuzawa, T. Ohta, H. Taguchi, 1982, Journal of biochemistry.

Comparison of primary structures and substrate specificities of two pullulan-hydrolyzing alpha-amylases, TVA I and TVA II, from Thermoactinomyces vulgaris R-47.

Y. Shimura, T. Tonozuka, Y. Sakano, 1995, Biochimica et biophysica acta.

Nucleotide sequence of the gene for aqualysin I (a thermophilic alkaline serine protease) of Thermus aquaticus YT-1 and characteristics of the deduced primary structure of the enzyme.

H. Matsuzawa, T. Ohta, I. Terada, 1988, European journal of biochemistry.

Expression of Aqualysin I under a Bacteriophage T 7 ( a Thermophilic Protease ) in Promoter Soluble Form in Escherichia coli

H. Matsuzawa, T. Ohta, I. Terada, 2018 .

Carboxypeptidase Taq, a thermostable zinc enzyme, from Thermus aquaticus YT-1: molecular cloning, sequencing, and expression of the encoding gene in Escherichia coli.

E. Yoshimura, H. Matsuzawa, S. Kaminogawa, 1994, Bioscience, biotechnology, and biochemistry.

Enhancement of the thermostability of subtilisin E by introduction of a disulfide bond engineered on the basis of structural comparison with a thermophilic serine protease.

M. Inouye, Y. Maeda, H. Matsuzawa, 1990, The Journal of biological chemistry.

Molecular cloning and nucleotide sequence of the gene for pyruvate kinase of Bacillus stearothermophilus and the production of the enzyme in Escherichia coli. Evidence that the genes for phosphofructokinase and pyruvate kinase constitute an operon.

H. Sakai, T. Ohta, 1993, European journal of biochemistry.

The role of guanosine 5'-triphosphate in the initiation of peptide synthesis. 3. Binding of formylmethionyl-tRNA to ribosomes.

R. Thach, T. Ohta, S. Sarkar, 1967, Proceedings of the National Academy of Sciences of the United States of America.

Nucleotide sequence of the rodA gene, responsible for the rod shape of Escherichia coli: rodA and the pbpA gene, encoding penicillin-binding protein 2, constitute the rodA operon

H. Matsuzawa, T. Ohta, S. Asoh, 1989, Journal of bacteriology.

Nucleotide sequence of the pbpA gene and characteristics of the deduced amino acid sequence of penicillin-binding protein 2 of Escherichia coli K12.

J. Strominger, F. Ishino, H. Matsuzawa, 1986, European journal of biochemistry.

Crystallization of and preliminary crystallographic data for allosteric L-lactate dehydrogenase from Bifidobacterium longum.

B. Mikami, S. Iwata, T. Minowa, 1989, Journal of biochemistry.

Fructose 1,6-bisphosphate-dependent L-lactate dehydrogenase from Thermus aquaticus YT-1, an extreme thermophile: activation by citrate and modification reagents and comparison with Thermus caldophilus GK24 L-lactate dehydrogenase.

M. Machida, H. Matsuzawa, T. Ohta, 1985, Journal of biochemistry.

Homotropic Activation via the Subunit Interaction and Allosteric Symmetry Revealed on Analysis of Hybrid Enzymes ofl-Lactate Dehydrogenase*

H. Matsuzawa, S. Fushinobu, T. Ohta, 1998, The Journal of Biological Chemistry.

T and R states in the crystals of bacterial L–lactate dehydrogenase reveal the mechanism for allosteric control

S. Iwata, T. Minowa, T. Ohta, 1994, Nature Structural Biology.

Molecular basis of allosteric activation of bacterial L-lactate dehydrogenase.

S. Iwata, T. Ohta, 1993, Journal of molecular biology.

Unusual amino acid substitution in the anion-binding site of Lactobacillus plantarum non-allosteric L-lactate dehydrogenase.

T. Ohta, H. Taguchi, 1992, European Journal of Biochemistry.

Mechanism of allosteric transition of bacterial L-lactate dehydrogenase.

S. Iwata, T. Minowa, T. Ohta, 1992, Faraday discussions.

Involvement of the conserved histidine-188 residue in the L-lactate dehydrogenase from Thermus caldophilus GK24 in allosteric regulation by fructose 1,6-bisphosphate.

H. Matsuzawa, T. Ohta, G. Schroeder, 1988, Biochemical and biophysical research communications.

Nucleotide sequence and characteristics of the gene for L-lactate dehydrogenase of Thermus caldophilus GK24 and the deduced amino-acid sequence of the enzyme.

M. Machida, H. Matsuzawa, T. Ohta, 1986, European journal of biochemistry.

Allosteric effect of fructose 1,6-bisphosphate on the conformation of NAD+ as bound to L-lactate dehydrogenase from Thermus caldophilus GK24.

S. Yokoyama, M. Machida, H. Matsuzawa, 1985, The Journal of biological chemistry.

Studies on the structure and function of subtilisin E by protein engineering.

M. Inouye, M. Yamasaki, H. Matsuzawa, 1996, Advances in experimental medicine and biology.

Nucleotide sequence and characteristics of the gene for L-lactate dehydrogenase of Thermus aquaticus YT-1 and the deduced amino acid sequence of the enzyme.

H. Matsuzawa, T. Ohta, M. Ono, 1990, Journal of biochemistry.

Amino acid residues in the allosteric site of L-lactate dehydrogenase from Bifidobacterium longum

S. Iwata, T. Minowa, H. Sakai, 1989 .

Conformation of NAD+ bound to allosteric L-lactate dehydrogenase activated by chemical modification.

S. Yokoyama, H. Matsuzawa, T. Ohta, 1989, The Journal of biological chemistry.

Identification of an allosteric site residue of a fructose 1,6‐bisphosphate‐dependent L‐lactate dehydrogenase of Thermus caldophilus GK24: production of a non‐allosteric form by protein engineering

M. Machida, H. Matsuzawa, T. Ohta, 1988 .

L-Lactate dehydrogenase from Thermus caldophilus GK24, an extremely thermophilic bacterium. Desensitization to fructose 1,6-bisphosphate in the activated state by arginine-specific chemical modification and the N-terminal amino acid sequence.

H. Matsuzawa, T. Ohta, H. Taguchi, 1984, European journal of biochemistry.

A Neopullulanase-type α-Amylase Gene from Thermoactinomyces vulgaris R-47

T. Tonozuka, Y. Sakano, H. Sakai, 1993 .

Synthesis of starch-graft-polyacrylonitrile hydrolyzate and its characterization

T. Ohta, Yasusato Sugahara, 2001 .

Glutamyl-tRNA synthetase from Thermus thermophilus HB8. Molecular cloning of the gltX gene and crystallization of the overproduced protein.

O. Nureki, K. Suzuki, S. Yokoyama, 1992, European journal of biochemistry.

Production of Thermophilic Extracellular Proteases (Aqualysins I and II) by Thermus aquaticus YT-1, an Extreme Thermophile

H. Matsuzawa, T. Ohta, M. Hamaoki, 1983 .

Colicin E8, a DNase which indicates an evolutionary relationship between colicins E2 and E3

H. Masaki, T. Ohta, M. Toba, 1988, Journal of bacteriology.

Colicin E 8 , a DNase Which Indicates an Evolutionary Relationship between Colicins E 2 and E 3

H. Masaki, T. Ohta, M. Toba, 2022 .

Purification and characterization of tyrosyl-RNA synthetase from baker's yeast.

T. Ohta, S. Kijima, K. Imahori, 1968, Journal of biochemistry.

Nucleic Acids Research

H. Masaki, T. Ohta, Departnent, 2014, Nucleic Acids Research.

Molecular cloning of a glucoamylase gene from a thermophilic Clostridium and kinetics of the cloned enzyme.

H. Sakai, T. Ohta, H. Kitamura, 1992, European journal of biochemistry.

Requirement of a COOH-terminal pro-sequence for the extracellular secretion of aqualysin I (a thermophilic subtilisin-type protease) in Thermus thermophilus.

H. Matsuzawa, T. Ohta, H. Taguchi, 1994, FEMS microbiology letters.

Fermentation conditions for efficient production of thermophilic protease in Escherichia coli harboring a plasmid

H. Matsuzawa, T. Ohta, S. Sakamoto, 1994, Applied Microbiology and Biotechnology.

Heat-stable extracellular proteolytic enzyme produced by Thermus caldophilus strain GK24, an extremely thermophilic bacterium.

H. Matsuzawa, T. Ohta, M. Hamaoki, 1983, Journal of biochemistry.

Conformational equilibrium of an enzyme catalytic site in the allosteric transition.

S. Yokoyama, H. Matsuzawa, T. Ohta, 1992, Biochemistry.

A 38 kDa precursor protein of aqualysin I (a thermophilic subtilisin‐type protease) with a C‐terminal extended sequence: its purification and in vitro processing

H. Matsuzawa, T. Ohta, K. Kurosaka, 1996, Molecular microbiology.

Structural Features of Bovine Mitochondrial tRNASerAGY Lacking the D Arm

T. Ueda, T. Ohta, Kimitsuna Watanabe, 1983 .

Site-directed mutants, at position 166, of RTEM-1 beta-lactamase that form a stable acyl-enzyme intermediate with penicillin.

H. Matsuzawa, T. Ohta, H. Adachi, 1991, The Journal of biological chemistry.

Molecular cloning of the genes for pyruvate kinase of two bacilli, Bacillus psychrophilus and Bacillus licheniformis, and comparison of the properties of the enzymes produced in Escherichia coli.

K. Tanaka, H. Matsuzawa, H. Sakai, 1995, Bioscience, biotechnology, and biochemistry.

Molecular Cloning of the Genes for Pyruvate Kinase of Two Bacilli , BaciUizspsychrophilns and BacMus tichenij 7 ormis , and Comparison of the Properties of the Enzymes Produced in Escheriehia cotit

H. Sakai, T. Ohta, Ken-ichi Tanaka, 2017 .

Junction of the 50S Ribosomal Subunit with the 30S Initiation Complex

D. Kolakofsky, R. Thach, T. Ohta, 1968, Nature.

Fluorometric investigation of the local conformation of 16S rRNA in the regions of the 3'- and 5'-ends.

T. Ohta, J. Kumagai, K. Imahori, 1976, Journal of biochemistry.

P1 specificity of aqualysin I (a subtilisin-type serine protease) from Thermus aquaticus YT-1, using P1-substituted derivatives of Streptomyces subtilisin inhibitor.

I. Kumagai, K. Miura, H. Matsuzawa, 1998, Bioscience, biotechnology, and biochemistry.

Substrate Specificity of Aqualysin I Altered by an Organic Solvent, DMSO.

H. Matsuzawa, T. Ohta, T. Tanaka, 1999, Bioscience, biotechnology, and biochemistry.

Involvement of NH2-terminal pro-sequence in the production of active aqualysin I (a thermophilic serine protease) in Escherichia coli.

H. Matsuzawa, T. Ohta, Y. Miyata, 1991, Agricultural and biological chemistry.

Determination of the positions of the disulfide bonds in aqualysin I (a thermophilic alkaline serine protease) of Thermus aquaticus YT-1.

H. Matsuzawa, T. Ohta, S. Kwon, 1988, Journal of biochemistry.

Stability of Thermostable Enzyme, Aqualysin I ; a Subtilisin-type Serine Protease from Thermus aquaticus YT-1.

H. Matsuzawa, T. Ohta, T. Tanaka, 1998, Bioscience, biotechnology, and biochemistry.

A convenient enzymatic synthesis of 4(2)-alpha-isomaltosylisomaltose using Thermoactinomyces vulgaris R-47 alpha-amylase II (TVA II).

T. Tonozuka, Y. Sakano, H. Sakai, 1994, Carbohydrate research.

A water‐soluble form of penicillin‐binding protein 2 of Escherichia coli constructed by site‐directed mutagenesis

H. Matsuzawa, T. Ohta, H. Adachi, 1987, FEBS letters.

The active site of carboxypeptidase Taq possesses the active-site motif His-Glu-X-X-His of zinc-dependent endopeptidases and aminopeptidases.

E. Yoshimura, Sang-Hyeon Lee, H. Matsuzawa, 1996, Protein engineering.

Purification and characterization of a thermostable carboxypeptidase (carboxypeptidase Taq) from Thermus aquaticus YT-1.

H. Matsuzawa, S. Kaminogawa, T. Ohta, 1992, Bioscience, biotechnology, and biochemistry.

The balance between different peptidoglycan precursors determines whether Escherichia coli cells will elongate or divide

B. Spratt, D. H. Edwards, H. Matsuzawa, 1990, Journal of bacteriology.

Allosteric and Kinetic Properties of L-Lactate Dehydrogenase from Thermus caldophilus GK24, an Extremely Thermophilic Bacterium

M. Machida, H. Matsuzawa, T. Ohta, 1985 .

Conformational change of tyrosyl-RNA synthetase induced by its specific transfer RNA.

T. Ohta, K. Imahori, I. Schimada, 1967, Journal of molecular biology.

Active-site residues of the transpeptidase domain of penicillin-binding protein 2 from Escherichia coli: similarity in catalytic mechanism to class A beta-lactamases.

H. Matsuzawa, T. Ohta, H. Adachi, 1992, Biochemistry.

Further Studies on rodA Mutant: a Round Morphological Mutant of Escherichia coli K-12 with Wild-Type Penicillin-Binding Protein 2

H. Matsuzawa, S. Tamaki, M. Matsuhashi, 1980 .

Isolation and characterization of a thermostable aminopeptidase(aminopeptidase T) from Thermus aquaticus YT-1, an extremely thermophilic bacterium.

H. Matsuzawa, S. Kaminogawa, T. Ohta, 1988 .

Roles of the N- and C- terminal pro-sequences of aqualysin I precursor in the processing and extracellular secretion of the enzyme.

H. Matsuzawa, T. Ohta, Y. C. Lee, 1996, Advances in experimental medicine and biology.